The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
Reads0
Chats0
TLDR
An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.Abstract:
Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria. This review focuses on the detailed structure of PBPs and their implication in peptidoglycan synthesis, maturation and recycling. An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.read more
Citations
More filters
Journal ArticleDOI
The Bacterial Cell Envelope
TL;DR: The bacteria cell envelope is a complex multilayered structure that serves to protect these organisms from their unpredictable and often hostile environment.
Journal ArticleDOI
Peptidoglycan structure and architecture
TL;DR: In several species examined, the fine structure of the peptidoglycan significantly varies with the growth conditions, and the different models for the architecture are discussed with respect to structural and physical parameters.
Journal ArticleDOI
The oyster genome reveals stress adaptation and complexity of shell formation
Guofan Zhang,Xiaodong Fang,Ximing Guo,Li Li,Ruibang Luo,Fei Xu,Pengcheng Yang,Linlin Zhang,Xiaotong Wang,Haigang Qi,Zhiqiang Xiong,Huayong Que,Yinlong Xie,Peter W. H. Holland,Jordi Paps,Yabing Zhu,Fucun Wu,Yuanxin Chen,Jiafeng Wang,Chunfang Peng,Jie Meng,Lan Yang,Jun Liu,Bo Wen,Na Zhang,Zhiyong Huang,Qihui Zhu,Yue Feng,Andrew S. Mount,Dennis Hedgecock,Zhe Xu,Yunjie Liu,Tomislav Domazet-Lošo,Yishuai Du,Xiaoqing Sun,Shoudu Zhang,Binghang Liu,Peizhou Cheng,Xuanting Jiang,Juan Li,Dingding Fan,Wei Wang,Wenjing Fu,Tong Wang,Bo Wang,Jibiao Zhang,Zhiyu Peng,Yingxiang Li,Na Li,Jinpeng Wang,Maoshan Chen,Yan He,Fengji Tan,Xiaorui Song,Qiumei Zheng,Ronglian Huang,Hailong Yang,Du Xuedi,Li Chen,Mei Yang,Patrick M. Gaffney,Shan Wang,Longhai Luo,Zhicai She,Yao Ming,Huang Wen,Shu Zhang,Baoyu Huang,Yong Zhang,Tao Qu,Peixiang Ni,Guoying Miao,Junyi Wang,Qiang Wang,Christian E. W. Steinberg,Haiyan Wang,Ning Li,Lumin Qian,Guojie Zhang,Yingrui Li,Huanming Yang,Xiao Liu,Jian Wang,Ye Yin,Jun Wang +84 more
TL;DR: The sequencing and assembly of the oyster genome using short reads and a fosmid-pooling strategy and transcriptomes of development and stress response and the proteome of the shell are reported, showing that shell formation in molluscs is more complex than currently understood and involves extensive participation of cells and their exosomes.
Journal ArticleDOI
Three Decades of β-Lactamase Inhibitors
TL;DR: In this paper, the authors review the catalytic mechanisms of each β-lactamase class and discuss approaches for circumventing β-latamase-mediated resistance, including properties and characteristics of mechanism-based inactivators.
Journal ArticleDOI
Bacterial peptidoglycan (murein) hydrolases.
TL;DR: The current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase is reviewed.
References
More filters
Journal ArticleDOI
The different shapes of cocci.
TL;DR: The present review aims to integrate older ultra-structural data with recent localization studies, in order to clarify the relation between the mechanisms of cell wall synthesis and the determination of cell shape in various cocci.
Journal ArticleDOI
Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.
TL;DR: Plausible hypotheses are put forward on the roles that the Penr protein fusions, acting as l,d-acyltransferases, may play in the (3→3) peptidoglycan-synthesizing molecular machines.
Journal ArticleDOI
Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation.
TL;DR: The authors' assay is shown to be a powerful instrument for an in vivo study of the interaction and assembly of proteins, as in the case of septum division formation.
Journal ArticleDOI
Penicillin Binding Protein 5 Affects Cell Diameter, Contour, and Morphology of Escherichia coli
David E. Nelson,Kevin D. Young +1 more
TL;DR: Among the low-molecular-weight PBPs, PBP 5 plays a principle role in determining cell diameter, surface uniformity, and overall topology of the peptidoglycan sacculus.
Journal ArticleDOI
Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli.
David E. Nelson,Kevin D. Young +1 more
TL;DR: The results further differentiate the roles of the low-molecular-weight PBPs, suggest a functional significance for the amphipathic membrane anchor of PBP 5 and, when combined with the recently determined crystal structure of P BP 5, suggest possible mechanisms by which these PBPs may contribute to maintenance of a uniform cell shape in E. coli.